Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Thaipisuttikul, I.; Hittle, L.E.; Chandra, R.; Zangari, D.; Dixon, C.L.; Garrett, T.A.; Rasko, D.A.; Dasgupta, N.; Moskowitz, S.M.; Malmstroem, L.; Goodlett, D.R.; Miller, S.I.; Bishop, R.E.; Ernst, R.K.
    A divergent Pseudomonas aeruginosa palmitoyltransferase essential for cystic fibrosis-specific lipid A (2014), Mol. Microbiol., 91, 158-174.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.3.1.251 Cyfos-7 phospholipase activity for PagP depends on presence of Triton X-100, dodecylmaltoside, or Cyfos-7 in decreasing order of specific activity Pseudomonas aeruginosa
2.3.1.251 dodecylmaltoside phospholipase activity for PagP depends on presence of Triton X-100, dodecylmaltoside, or Cyfos-7 in decreasing order of specific activity Pseudomonas aeruginosa
2.3.1.251 Triton X-100 phospholipase activity for PagP depends on presence of Triton X-100, dodecylmaltoside, or Cyfos-7 in decreasing order of specific activity. Triton X-100 participates as a substrate in the palmitoyltransferase reaction Pseudomonas aeruginosa

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.251 D84A mutation does not alter protein function Pseudomonas aeruginosa
2.3.1.251 D84N mutation does not alter protein function Pseudomonas aeruginosa
2.3.1.251 D86A mutation does not alter protein function Pseudomonas aeruginosa
2.3.1.251 D86N mutation does not alter protein function Pseudomonas aeruginosa
2.3.1.251 H35F loss of catalytic activity Pseudomonas aeruginosa
2.3.1.251 H35N loss of catalytic activity Pseudomonas aeruginosa
2.3.1.251 H45F mutation does not alter protein function Pseudomonas aeruginosa
2.3.1.251 S85A mutation does not alter protein function Pseudomonas aeruginosa
2.3.1.251 S85G mutation does not alter protein function Pseudomonas aeruginosa
2.3.1.251 S87A mutation does not alter protein function Pseudomonas aeruginosa
2.3.1.251 S87G mutation does not alter protein function Pseudomonas aeruginosa

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.251 Pseudomonas aeruginosa Q9I401
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.251 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + hexa-acyl lipid A
-
Pseudomonas aeruginosa 2-acyl-sn-glycero-3-phosphocholine + hepta-acyl lipid A
-
?
2.3.1.251 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + lipid IVA
-
Pseudomonas aeruginosa 2-acyl-sn-glycero-3-phosphocholine + lipid IVB
-
?
2.3.1.251 additional information enzyme from Pseudomonas aeruginosa transfers palmitates to the lipid A C-3' positions Pseudomonas aeruginosa ?
-
?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.251 PA1343
-
Pseudomonas aeruginosa